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Information on EC 1.14.11.67 - [histone H3]-trimethyl-L-lysine4 demethylase and Organism(s) Sus scrofa and UniProt Accession A1YVX4

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IUBMB Comments
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.
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Sus scrofa
UNIPROT: A1YVX4
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
kdm5b, jarid2, kdm5c, jarid1b, kdm5a, fbxl10, lysine-specific demethylase, jarid1c, jarid1a, kdm5d, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
histone H3-K4 demethylase
-
AOF1
-
-
KDM1
-
-
LSD1
-
-
lysine-specific demethylase 1
-
-
SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine4,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
histone H3-K4 demethylase is restricted to the corpus luteum
Manually annotated by BRENDA team
H3-K4 mono-, di-, and tri-methylation in large luteal cells increases as differentiation evolves but remains low in small luteal cells
Manually annotated by BRENDA team
cellular and follicular stage-specific patterns of histone H3 methylation at lysine 4 in porcine preovulatory follicles and during luteinization in pig ovaries, overview. LSD1/KDM1 expression is restricted to the corpus luteum. While granulosa cells of primary, secondary, and early antral follicles are negative for H3-K4 methylation those from large antral follicles show a striking upregulation in the cells located in the proximity to the oocyte
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
attenuation of isoforms KDM5B and KDM5C mRNA hampers embryo development to the blastocyst stage in fertilized, parthenogenetically activated and nuclear transfer embryos. Isoform KDM5B attenuation increases H3K4me2-3 levels on D3 embryos and H3K4 mono-, di- and trimethylation on D5 embryos.KDM5C attenuation increases H3K9me1 on D3 embryos, and H3K9me1 and H3K4me1 on D5 embryos. KDM5B and KDM5C attenuation affects DNA damage response and increases DNA double-strand breaks, and decreases development of UV-irradiated embryos
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDM5C_PIG
1516
0
170584
Swiss-Prot
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seneda, M.M.; Godmann, M.; Murphy, B.D.; Kimmins, S.; Bordignon, V.
Developmental regulation of histone H3 methylation at lysine 4 in the porcine ovary
Reproduction
135
829-838
2008
Sus scrofa, Sus scrofa (A1YVX4)
Manually annotated by BRENDA team
Glanzner, W.G.; Gutierrez, K.; Rissi, V.B.; de Macedo, M.P.; Lopez, R.; Currin, L.; Dicks, N.; Baldassarre, H.; Agellon, L.B.; Bordignon, V.
Histone lysine demethylases KDM5B and KDM5C modulate genome activation and stability in porcine embryos
Front. Cell Dev. Biol.
8
151
2020
Sus scrofa, Sus scrofa (A1YVX4)
Manually annotated by BRENDA team